9EP9

NMR solution structure of lipid transfer protei Sola l7 from tomato seeds

Summary for 9EP9

• Entry DOI: 10.2210/pdb9ep9/pdb
• NMR Information: BMRB: 34910
• Descriptor: Non-specific lipid-transfer protein (1 entity in total)
• Functional Keywords: lipid transfer protein fatty acids, allergen
• Biological source: Solanum lycopersicum (tomato)
• Total number of polymer chains: 1
• Total formula weight: 9453.61

Authors

Parron-Ballesteros, J.,Mantin-Pedraz, L.,G.Gordo, R.,Mayorga, C.,Villaba, M.,Batanero, E.,Pantoja-Uceda, D.,Turnay, J. (deposition date: 2024-03-18, release date: 2024-09-04, Last modification date: 2024-10-09)

Primary citation

Parron-Ballesteros, J.,Martin-Pedraza, L.,Gordo, R.G.,Mayorga, C.,Pastor-Vargas, C.,Titaux-Delgado, G.A.,Villalba, M.,Batanero, E.,Pantoja-Uceda, D.,Turnay, J.
Long-chain fatty acids block allergic reaction against lipid transfer protein Sola l 7 from tomato seeds.
Protein Sci., 33:e5154-e5154, 2024

PubMed Abstract: Due to the benefits of tomato as an antioxidant and vitamin source, allergy to this vegetable food is a clinically concerning problem. Sola l 7, a class I lipid transfer protein found in tomato seeds, has been identified as an allergen linked to severe anaphylaxis. However, the role of lipid binding in Sola l 7-induced allergy remains unclear. Here, the three-dimensional structure of recombinant Sola l 7 (rSola l 7) has been elucidated using nuclear magnetic resonance spectroscopy (NMR). Its interaction with free fatty acids has been deeply studied; fluorescence emission spectroscopy revealed that different long-chain fatty acids interact with the protein, affecting the only tyrosine residue present in Sola l 7. On the contrary, no changes in the overall secondary structure were observed after the analysis of the circular dichroism spectra in the presence of fatty acids. Unsaturated oleic and linoleic fatty acids presented higher affinity and promoted more significant changes than saturated or short-chain fatty acids. H-N HSQC NMR spectra allowed to determine the regions of the protein that were modified when rSola l 7 interacts with the fatty acids, suggesting epitope modification after the interaction. For corroboration, IgG and IgE binding to rSola l 7 were assessed in the presence of free fatty acids, revealing that both IgE and IgG binding were significantly lower than in their absence, suggesting a potential protective role of unsaturated fatty acids in tomato allergy.

PubMed: 39180496
DOI: 10.1002/pro.5154

Experimental method

SOLUTION NMR